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Volumn 38, Issue 5-6, 2005, Pages 189-200

Phosphoglycerate kinase inhibits epithelial cell invasion by group B streptococci

Author keywords

Actinin; Actin; Actin binding proteins; Group B streptococcus; HeLa cells; Phosphoglycerate kinase

Indexed keywords

ACTIN BINDING PROTEIN; ALPHA ACTININ; F ACTIN; PHOSPHOGLYCERATE KINASE;

EID: 19544389507     PISSN: 08824010     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micpath.2005.02.002     Document Type: Article
Times cited : (21)

References (60)
  • 2
    • 0028236084 scopus 로고
    • Multistate case-control study of maternal risk factors for neonatal group B streptococcal disease. The Active Surveillance Study Group
    • A. Schuchat, K. Deaver-Robinson, B.D. Plikaytis, K.M. Zangwell, J. Mohle-Boetani, and J.D. Wegner Multistate case-control study of maternal risk factors for neonatal group B streptococcal disease. The Active Surveillance Study Group Pediatr Infect Dis J 13 1994 623 629
    • (1994) Pediatr Infect Dis J , vol.13 , pp. 623-629
    • Schuchat, A.1    Deaver-Robinson, K.2    Plikaytis, B.D.3    Zangwell, K.M.4    Mohle-Boetani, J.5    Wegner, J.D.6
  • 3
    • 0031875613 scopus 로고    scopus 로고
    • Epidemiology of group B streptococcal disease in the United States: Shifting paradigms
    • A. Schuchat Epidemiology of group B streptococcal disease in the United States: shifting paradigms Clin Microbiol Rev 11 1998 497 513
    • (1998) Clin Microbiol Rev , vol.11 , pp. 497-513
    • Schuchat, A.1
  • 4
    • 0027308989 scopus 로고
    • A population-based assessment of invasive disease due to group B streptococcus in nonpregnant adults
    • M.M. Farley, R.C. Harvey, T. Studll, J.D. Smith, A. Schuchat, and J.D. Wenger A population-based assessment of invasive disease due to group B streptococcus in nonpregnant adults N Engl J Med 328 1993 1087 1811
    • (1993) N Engl J Med , vol.328 , pp. 1087-1811
    • Farley, M.M.1    Harvey, R.C.2    Studll, T.3    Smith, J.D.4    Schuchat, A.5    Wenger, J.D.6
  • 5
    • 0033914786 scopus 로고    scopus 로고
    • Invasive disease due to group B streptococcal infection in adults: Results from a Canadian population-based active surveillance study - 1996
    • G.J. Tyrrell, L. Senzilet, J. Spika, D. Kertesz, J. Talbot, M. Alagartnam, and The sentinel Health Surveillance System Site Coordinators Invasive disease due to group B streptococcal infection in adults: results from a Canadian population-based active surveillance study - 1996 J Infect Dis 182 2000 168 173
    • (2000) J Infect Dis , vol.182 , pp. 168-173
    • Tyrrell, G.J.1    Senzilet, L.2    Spika, J.3    Kertesz, D.4    Talbot, J.5    Alagartnam, M.6
  • 6
  • 7
    • 0028957862 scopus 로고
    • Group B streptococci adhere to a variant of fibronectin attached to a solid phase
    • G.S. Tamura, and C.E. Rubens Group B streptococci adhere to a variant of fibronectin attached to a solid phase Mol Microbiol 15 1995 581 589
    • (1995) Mol Microbiol , vol.15 , pp. 581-589
    • Tamura, G.S.1    Rubens, C.E.2
  • 8
    • 0036266052 scopus 로고    scopus 로고
    • Identification of novel adhesions from group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding
    • C. Beckmann, J.D. Waggoner, T.O. Harris, G.S. Tamura, and C.E. Rubens Identification of novel adhesions from group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding Infect Immun 70 2002 2869 2876
    • (2002) Infect Immun , vol.70 , pp. 2869-2876
    • Beckmann, C.1    Waggoner, J.D.2    Harris, T.O.3    Tamura, G.S.4    Rubens, C.E.5
  • 9
    • 0034019163 scopus 로고    scopus 로고
    • Group B streptococci and other gram-positive cocci bind cytokeratin 8
    • G.S. Tamura, and A. Nittayajarn Group B streptococci and other gram-positive cocci bind cytokeratin 8 Infect Immun 68 2000 2129 2134
    • (2000) Infect Immun , vol.68 , pp. 2129-2134
    • Tamura, G.S.1    Nittayajarn, A.2
  • 10
    • 0032486286 scopus 로고    scopus 로고
    • α-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • V. Pancholi, and V.A. Fischetti α-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci J Biol Chem 273 1998 14503 14515
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 11
    • 0036117970 scopus 로고    scopus 로고
    • The group B streptococcal C5a peptidase is both a specific protease and an invasin
    • Q. Cheng, D. Stafslein, S.S. Purushothaman, and P. Cleary The group B streptococcal C5a peptidase is both a specific protease and an invasin Infect Immun 70 2002 2408 2413
    • (2002) Infect Immun , vol.70 , pp. 2408-2413
    • Cheng, Q.1    Stafslein, D.2    Purushothaman, S.S.3    Cleary, P.4
  • 12
    • 0141834741 scopus 로고    scopus 로고
    • Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: Surface localization, enzymatic activity, and protein-protein interactions
    • K.N. Siefert, W.P. McArthur, A.S. Bleiweis, and L.J. Brady Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions Can J Microbiol 49 2003 350 356
    • (2003) Can J Microbiol , vol.49 , pp. 350-356
    • Siefert, K.N.1    McArthur, W.P.2    Bleiweis, A.S.3    Brady, L.J.4
  • 13
    • 0029799009 scopus 로고    scopus 로고
    • The plasmin-binding protein of Plr of group a streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase
    • S.B. Winram, and R. Lottenberg The plasmin-binding protein of Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase Microbiology 142 1996 2311 2320
    • (1996) Microbiology , vol.142 , pp. 2311-2320
    • Winram, S.B.1    Lottenberg, R.2
  • 14
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen binding protein
    • S. Bergmann, M. Rohde, and S. Hammerschmidt Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen binding protein Infect Immun 72 2004 2419 2426
    • (2004) Infect Immun , vol.72 , pp. 2419-2426
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 15
    • 0034883769 scopus 로고    scopus 로고
    • De novo formation of focal complex-like structures in host cells by invading streptococci
    • V. Ozeri, I. Rosenshine, A. Ben-Ze'ev, G.M. Bokoch, T. Jou, and E. Hanski De novo formation of focal complex-like structures in host cells by invading streptococci Mol Microbiol 41 2001 561 573
    • (2001) Mol Microbiol , vol.41 , pp. 561-573
    • Ozeri, V.1    Rosenshine, I.2    Ben-Ze'Ev, A.3    Bokoch, G.M.4    Jou, T.5    Hanski, E.6
  • 16
    • 0036952406 scopus 로고    scopus 로고
    • Binding and invasion of HeLa and MRC-5 cells by Streptococcus agalactiae
    • G.J. Tyrrell, A. Kennedy, S.E. Shokoples, and R.K. Sherburne Binding and invasion of HeLa and MRC-5 cells by Streptococcus agalactiae Microbiology 148 2002 3921 3931
    • (2002) Microbiology , vol.148 , pp. 3921-3931
    • Tyrrell, G.J.1    Kennedy, A.2    Shokoples, S.E.3    Sherburne, R.K.4
  • 18
    • 0036210840 scopus 로고    scopus 로고
    • The actin filament architecture: Tightly regulated by the cells, manipulated by pathogens
    • M.R. Ahmadian, A. Wittinhofer, and G. Schmidt The actin filament architecture: tightly regulated by the cells, manipulated by pathogens EMBO Rep 3 2002 214 218
    • (2002) EMBO Rep , vol.3 , pp. 214-218
    • Ahmadian, M.R.1    Wittinhofer, A.2    Schmidt, G.3
  • 19
    • 0027518389 scopus 로고
    • Group B streptococci invade endothelial cells: Type III capsular polysaccharide attenuates invasion
    • R.L. Gibson, M.K. Lee, C. Soderland, E.Y. Chi, and C.E. Rubens Group B streptococci invade endothelial cells: type III capsular polysaccharide attenuates invasion Infect Immun 61 1993 478 485
    • (1993) Infect Immun , vol.61 , pp. 478-485
    • Gibson, R.L.1    Lee, M.K.2    Soderland, C.3    Chi, E.Y.4    Rubens, C.E.5
  • 21
    • 0033870279 scopus 로고    scopus 로고
    • Interactions between Streptococcus suis serotype 2 and different epithelial cell lines
    • M. Lalond, M. Segura, S. Lacouture, and M. Gottschalk Interactions between Streptococcus suis serotype 2 and different epithelial cell lines Microbiology 146 2000 1913 1921
    • (2000) Microbiology , vol.146 , pp. 1913-1921
    • Lalond, M.1    Segura, M.2    Lacouture, S.3    Gottschalk, M.4
  • 22
    • 0029756760 scopus 로고    scopus 로고
    • Uptake of Streptococcus pneumoniae by respiratory epithelial cells
    • U.M. Talbot, A.W. Paton, and J.C. Paton Uptake of Streptococcus pneumoniae by respiratory epithelial cells Infect Immun 64 1996 3772 3777
    • (1996) Infect Immun , vol.64 , pp. 3772-3777
    • Talbot, U.M.1    Paton, A.W.2    Paton, J.C.3
  • 23
    • 0031784557 scopus 로고    scopus 로고
    • Characterization of mechanisms involved in uptake of Streptococcus dysgalactiae by bovine mammary epithelial cells
    • L.F. Calvinho, and S.P. Oliver Characterization of mechanisms involved in uptake of Streptococcus dysgalactiae by bovine mammary epithelial cells Vet Microbiol 63 1998 261 274
    • (1998) Vet Microbiol , vol.63 , pp. 261-274
    • Calvinho, L.F.1    Oliver, S.P.2
  • 25
    • 0032904116 scopus 로고    scopus 로고
    • High frequency intracellular invasion of epithelial cells by serotype M1 group a streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements
    • P.E. Dombeck, D. Cue, J. Sedgewick, H. Lam, S. Ruschkowski, B.B. Finaly, and P.P. Clearly High frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements Mol Microbiol 31 1999 859 870
    • (1999) Mol Microbiol , vol.31 , pp. 859-870
    • Dombeck, P.E.1    Cue, D.2    Sedgewick, J.3    Lam, H.4    Ruschkowski, S.5    Finaly, B.B.6    Clearly, P.P.7
  • 26
    • 0037225490 scopus 로고    scopus 로고
    • The alpha-actinin gene family: A revised classification
    • J.D. Dixson, M.R.J. Forstner, and D.M. Garcia The alpha-actinin gene family: a revised classification J Mol Evol 56 2003 1 10
    • (2003) J Mol Evol , vol.56 , pp. 1-10
    • Dixson, J.D.1    Forstner, M.R.J.2    Garcia, D.M.3
  • 27
    • 0032054640 scopus 로고    scopus 로고
    • F-actin-binding proteins
    • A. McGough F-actin-binding proteins Curr Opin Struct Biol 8 1998 166 176
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 166-176
    • McGough, A.1
  • 29
    • 0036369218 scopus 로고    scopus 로고
    • Mechanisms of EF-Tu, a pioneer GTPase
    • I.M. Krab, and A. Parmeggiani Mechanisms of EF-Tu, a pioneer GTPase Prog Nucl Acid Res 71 2002 513 551
    • (2002) Prog Nucl Acid Res , vol.71 , pp. 513-551
    • Krab, I.M.1    Parmeggiani, A.2
  • 31
    • 0015222181 scopus 로고
    • Quantitative comparison of the binding of various glycolytic enzymes to F-actin and the interaction of aldolase with G-actin
    • H. Arnold, R. Henning, and D. Pette Quantitative comparison of the binding of various glycolytic enzymes to F-actin and the interaction of aldolase with G-actin Eur J Biochem 22 1971 121 126
    • (1971) Eur J Biochem , vol.22 , pp. 121-126
    • Arnold, H.1    Henning, R.2    Pette, D.3
  • 32
    • 0019814008 scopus 로고
    • Interaction of muscle glycolytic enzymes with thin filament proteins
    • W.W. Bronstein, and H.R. Knull Interaction of muscle glycolytic enzymes with thin filament proteins Can J Biochem 59 1981 494 499
    • (1981) Can J Biochem , vol.59 , pp. 494-499
    • Bronstein, W.W.1    Knull, H.R.2
  • 34
    • 0030964241 scopus 로고    scopus 로고
    • Exploitation of mammalian host cell functions by bacterial pathogens
    • B.B. Finlay, and P. Cossart Exploitation of mammalian host cell functions by bacterial pathogens Science 276 1997 718 725
    • (1997) Science , vol.276 , pp. 718-725
    • Finlay, B.B.1    Cossart, P.2
  • 35
    • 0037452070 scopus 로고    scopus 로고
    • Microbial pathogenesis and cytoskeletal function
    • S. Gruenheid, and B.B. Finlay Microbial pathogenesis and cytoskeletal function Nature 422 2003 775 781
    • (2003) Nature , vol.422 , pp. 775-781
    • Gruenheid, S.1    Finlay, B.B.2
  • 36
    • 0037406727 scopus 로고    scopus 로고
    • Coordinate regulation of Salmonella enterica serovar Typhimurium invasion of epithelial cells by the Arp 2/3 complex and Rho GTPases
    • A.K. Criss, and J.E. Casanova Coordinate regulation of Salmonella enterica serovar Typhimurium invasion of epithelial cells by the Arp 2/3 complex and Rho GTPases Infect Immun 71 2003 2885 2891
    • (2003) Infect Immun , vol.71 , pp. 2885-2891
    • Criss, A.K.1    Casanova, J.E.2
  • 37
    • 6344241120 scopus 로고    scopus 로고
    • Analysis of the mechanisms of Salmonella-induced actin assembly during invasion of host cells and intracellular replication
    • K.E. Unsworth, M. Way, M. McNiven, L. Machesky, and D.W. Holden Analysis of the mechanisms of Salmonella-induced actin assembly during invasion of host cells and intracellular replication Cell Microbiol 2004 doi: 10.1111/j.1462-5822.2004.00417.x
    • (2004) Cell Microbiol
    • Unsworth, K.E.1    Way, M.2    McNiven, M.3    MacHesky, L.4    Holden, D.W.5
  • 38
    • 0033962672 scopus 로고    scopus 로고
    • Focal adhesions - The cytoskeletal connection
    • D.R. Critchely Focal adhesions - the cytoskeletal connection Curr Opin Cell Biol 12 2000 133 139
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 133-139
    • Critchely, D.R.1
  • 39
    • 0036535898 scopus 로고    scopus 로고
    • The cytoplasmic face of cell contact sites
    • S. Pokutta, and W.I. Weis The cytoplasmic face of cell contact sites Curr Opin Struct Biol 12 2002 255 262
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 255-262
    • Pokutta, S.1    Weis, W.I.2
  • 40
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation
    • B.E. Bernstein, P.A.M. Michels, and W.G.J. Hol Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation Nature 385 1997 275 278
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.M.2    Hol, W.G.J.3
  • 41
    • 1842301085 scopus 로고    scopus 로고
    • 3-Phosphoglycerrate kinase: A glycolytic enzyme protein present in the cell wall of Candida albicans
    • H.M. Alloush, J.L. Lopze-Ribot, B.J. Masetn, and W.L. Chaffin 3-Phosphoglycerrate kinase: a glycolytic enzyme protein present in the cell wall of Candida albicans Microbiology 143 1997 321 330
    • (1997) Microbiology , vol.143 , pp. 321-330
    • Alloush, H.M.1    Lopze-Ribot, J.L.2    Masetn, B.J.3    Chaffin, W.L.4
  • 42
    • 0029001394 scopus 로고
    • Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni and characterization of its gene products
    • W.L. Keung, K.A. Shalaby, A. Thankur, A.M. Medhat, A.M. Karim, and P.T. LoVerde Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni and characterization of its gene products Mol Biochem Parasitol 71 1995 221 231
    • (1995) Mol Biochem Parasitol , vol.71 , pp. 221-231
    • Keung, W.L.1    Shalaby, K.A.2    Thankur, A.3    Medhat, A.M.4    Karim, A.M.5    Loverde, P.T.6
  • 43
    • 0028803091 scopus 로고
    • Immune response to Schistosoma masoni phosphoglycerate kinase during natural and experimental infection: Identification of a schistosome-specific B-cell epitope
    • K.W. Lee, A. Thakur, A.M. Karim, and P.T. LoVerde Immune response to Schistosoma masoni phosphoglycerate kinase during natural and experimental infection: identification of a schistosome-specific B-cell epitope Infect Immun 63 1995 4307 4311
    • (1995) Infect Immun , vol.63 , pp. 4307-4311
    • Lee, K.W.1    Thakur, A.2    Karim, A.M.3    Loverde, P.T.4
  • 44
    • 0026682564 scopus 로고
    • A major outer surface protein on group a streptococci is a glyceraldehyde-3-phosophate-dehydrogenase with multiple binding activity
    • V. Pancholi, and V.A. Fischetti A major outer surface protein on group A streptococci is a glyceraldehyde-3-phosophate-dehydrogenase with multiple binding activity J Exp Med 176 1992 415 426
    • (1992) J Exp Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 45
    • 0027249488 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase on the surface of group a streptococci is also an ADP-ribosylating enzyme
    • V. Pancholi, and V.A. Fishetti Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme Proc Natl Acad Sci USA 90 1993 8154 8158
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8154-8158
    • Pancholi, V.1    Fishetti, V.A.2
  • 46
    • 0031014279 scopus 로고    scopus 로고
    • Cloning of the glutamine synthetase gene from group B streptococci
    • A.N. Suvorov, A.E. Flores, and P. Ferrieri Cloning of the glutamine synthetase gene from group B streptococci Infect Immun 65 1997 191 196
    • (1997) Infect Immun , vol.65 , pp. 191-196
    • Suvorov, A.N.1    Flores, A.E.2    Ferrieri, P.3
  • 52
    • 0027189729 scopus 로고
    • Actin is a surface component of calf pulmonary endothelial cells in culture
    • J. Moroianu, J.W. Fett, J.F. Roirdan, and B.L. Vallee Actin is a surface component of calf pulmonary endothelial cells in culture Proc Natl Acad Sci USA 90 1993 3815 3819
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3815-3819
    • Moroianu, J.1    Fett, J.W.2    Roirdan, J.F.3    Vallee, B.L.4
  • 53
    • 0024453809 scopus 로고
    • Brain capillary 46 000 Dalton protein is cytoplasmic actin and is localized to endothelial plasma membrane
    • W.M. Paridge, D.M. Nowlin, T.B. Choi, J. Yang, J. Calacay, and J.E. Shively Brain capillary 46 000 Dalton protein is cytoplasmic actin and is localized to endothelial plasma membrane J Cereb Blood Flow Metab 9 1989 657 680
    • (1989) J Cereb Blood Flow Metab , vol.9 , pp. 657-680
    • Paridge, W.M.1    Nowlin, D.M.2    Choi, T.B.3    Yang, J.4    Calacay, J.5    Shively, J.E.6
  • 55
    • 0034383951 scopus 로고    scopus 로고
    • The interaction of titin and α-actinin is controlled by a phospholipids-regulated intramolecular pseudoligand mechanism
    • P. Young, and M. Gautel The interaction of titin and α-actinin is controlled by a phospholipids-regulated intramolecular pseudoligand mechanism EMBO J 19 2000 6331 6340
    • (2000) EMBO J , vol.19 , pp. 6331-6340
    • Young, P.1    Gautel, M.2
  • 56
    • 0028050414 scopus 로고
    • Phosphatidylinositol 3-kinase binds to alpha-actinin through the p85 subunit
    • F. Shibaskaki, K. Fukami, Y. Fukui, and T. Takenawa Phosphatidylinositol 3-kinase binds to alpha-actinin through the p85 subunit Biochem J 302 1994 551 557
    • (1994) Biochem J , vol.302 , pp. 551-557
    • Shibaskaki, F.1    Fukami, K.2    Fukui, Y.3    Takenawa, T.4
  • 58
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • G. Towbin, T. Staehelin, and J. Gordon Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Proc Natl Acad Sci USA. 76 1979 4350 4354
    • (1979) Proc Natl Acad Sci USA. , vol.76 , pp. 4350-4354
    • Towbin, G.1    Staehelin, T.2    Gordon, J.3
  • 60
    • 0026460955 scopus 로고
    • Respiratory epithelial cell invasion by group B streptococci
    • C.E. Rubens, S. Smith, M. Hulse, E.Y. Chi, and G. Van Belle Respiratory epithelial cell invasion by group B streptococci Infect Immun 60 1992 5157 5163
    • (1992) Infect Immun , vol.60 , pp. 5157-5163
    • Rubens, C.E.1    Smith, S.2    Hulse, M.3    Chi, E.Y.4    Van Belle, G.5


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